0000000001185368

AUTHOR

Alessandra Maria Vitale

showing 8 related works from this author

Molecular Chaperones and Thyroid Cancer

2021

Thyroid cancers are the most common of the endocrine system malignancies and progress must be made in the areas of differential diagnosis and treatment to improve patient management. Advances in the understanding of carcinogenic mechanisms have occurred in various fronts, including studies of the chaperone system (CS). Components of the CS are found to be quantitatively increased or decreased, and some correlations have been established between the quantitative changes and tumor type, prognosis, and response to treatment. These correlations provide the basis for identifying distinctive patterns useful in differential diagnosis and for planning experiments aiming at elucidating the role of t…

QH301-705.5thyroid tumorsHsp90Reviewmedicine.disease_causeCatalysisChaperoninHsp70Inorganic ChemistryHsp27chaperone systemdifferential diagnosismedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsThyroid NeoplasmsBiology (General)Physical and Theoretical ChemistryHsp27QD1-999Molecular BiologyThyroid cancerSpectroscopychaperonotherapybiologychaperonopathies by mistakeOrganic ChemistryThyroidmolecular chaperonesChaperonin 60General Medicinemedicine.diseaseHsp60Hsp90Computer Science ApplicationsChemistrymedicine.anatomical_structureChaperone (protein)biology.proteinCancer researchHSP60CarcinogenesisInternational Journal of Molecular Sciences
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Air Pollution: Role of Extracellular Vesicles-Derived Non-Coding RNAs in Environmental Stress Response

2023

Air pollution has increased over the years, causing a negative impact on society due to the many health-related problems it can contribute to. Although the type and extent of air pollutants are known, the molecular mechanisms underlying the induction of negative effects on the human body remain unclear. Emerging evidence suggests the crucial involvement of different molecular mediators in inflammation and oxidative stress in air pollution-induced disorders. Among these, non-coding RNAs (ncRNAs) carried by extracellular vesicles (EVs) may play an essential role in gene regulation of the cell stress response in pollutant-induced multiorgan disorders. This review highlights EV-transported ncRN…

liquid biopsystreair pollutionnon-coding RNAheat shock proteinbiomarkerextracellular vesiclepersonalized medicineGeneral MedicineCells
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Quantitative immunomorphological analysis of heat shock proteins in thyroid follicular adenoma and carcinoma tissues reveals their potential for diff…

2019

Hsp27, Hsp60, Hsp70, and Hsp90 are chaperones that play a crucial role in cellular homeostasis and differentiation, but they may be implicated in carcinogenesis. Follicular neoplasms of the thyroid include follicular adenoma and follicular carcinoma. The former is a very frequent benign encapsulated nodule, whereas the other is a nodule that infiltrates the capsule, blood vessels and the adjacent parenchyma, with a tendency to metastasize. The main objective was to assess the potential of the Hsps in differential diagnosis and carcinogenesis. We quantified by immunohistochemistry Hsp27, Hsp60, Hsp70, and Hsp90 on thin sections of human thyroid tissue with follicular adenoma or follicular ca…

0301 basic medicinePathologyCellular homeostasismedicine.disease_causechaperonopathieslcsh:TechnologyHsp70lcsh:Chemistry0302 clinical medicineFollicular phasedifferential diagnosisGeneral Materials ScienceHsp27Instrumentationlcsh:QH301-705.5CarcinogenesiFluid Flow and Transfer ProcessesThyroidThyroidGeneral EngineeringHsp60Follicular adenomalcsh:QC1-999Computer Science Applicationsmedicine.anatomical_structure030220 oncology & carcinogenesisMolecular chaperoneImmunohistochemistrycarcinogenesismedicine.medical_specialtyendocrine systemanimal structuresAdenomaDifferential diagnosiHsp90BiologyFollicular carcinoma03 medical and health sciencesParenchymaCarcinomamedicinelcsh:TProcess Chemistry and Technologymedicine.disease030104 developmental biologylcsh:Biology (General)lcsh:QD1-999lcsh:TA1-2040ChaperonopathieCarcinogenesislcsh:Engineering (General). Civil engineering (General)lcsh:Physics
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Muscle Histopathological Abnormalities in a Patient With a CCT5 Mutation Predicted to Affect the Apical Domain of the Chaperonin Subunit.

2022

Recognition of diseases associated with mutations of the chaperone system genes, e.g., chaperonopathies, is on the rise. Hereditary and clinical aspects are established, but the impact of the mutation on the chaperone molecule and the mechanisms underpinning the tissue abnormalities are not. Here, histological features of skeletal muscle from a patient with a severe, early onset, distal motor neuropathy, carrying a mutation on the CCT5 subunit (MUT) were examined in comparison with normal muscle (CTR). The MUT muscle was considerably modified; atrophy of fibers and disruption of the tissue architecture were prominent, with many fibers in apoptosis. CCT5 was diversely present in the sarcolem…

Settore BIO/17 - IstologiaCCT5 neurochaperonopathies chaperonin neurodegenerative diseases neuropathies chaperone system muscle histopathology CCT5 apical domainSettore MED/38 - Pediatria Generale E SpecialisticaSettore BIO/16 - Anatomia UmanaSettore MED/30 - Malattie Apparato VisivoBiochemistry Genetics and Molecular Biology (miscellaneous)Molecular BiologyBiochemistrySettore CHIM/02 - Chimica FisicaFrontiers in molecular biosciences
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Structural and Dynamic Disturbances Revealed by Molecular Dynamics Simulations Predict the Impact on Function of CCT5 Chaperonin Mutations Associated…

2023

Mutations in genes encoding molecular chaperones, for instance the genes encoding the subunits of the chaperonin CCT (chaperonin containing TCP-1, also known as TRiC), are associated with rare neurodegenerative disorders. Using a classical molecular dynamics approach, we investigated the occurrence of conformational changes and differences in physicochemical properties of the CCT5 mutations His147Arg and Leu224Val associated with a sensory and a motor distal neuropathy, respectively. The apical domain of both variants was substantially but differently affected by the mutations, although these were in other domains. The distribution of hydrogen bonds and electrostatic potentials on the surfa…

Settore BIO/16 - Anatomia UmanaOrganic ChemistryCCT5 mutationsGeneral Medicineprotein bindingCatalysisComputer Science ApplicationsInorganic Chemistryelectrostatic potentialCCT5 chaperonopathieschaperone systemhydrogen bondsPhysical and Theoretical ChemistryCCT5Molecular BiologySpectroscopyapical domainSettore CHIM/02 - Chimica Fisica
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Missense Mutations of Human Hsp60: A Computational Analysis to Unveil Their Pathological Significance

2020

Two chaperonopathies have been linked to mutations in the human hsp60 (hHsp60; HSPD1) gene, but other existing variants might cause diseases, even if there is no comprehensive information about this possibility. To fill this vacuum, which might be at the basis of misdiagnoses or simply ignorance of chaperonopathies in patients who would benefit by proper identification of their ailments, we searched the sequenced human genomes available in public databases to determine the range of missense mutations in the single hsp60 gene. A total of 224 missense mutations were identified, including those already characterized. Detailed examination of these mutations was carried out to assess their possi…

0301 basic medicineHsp60 gene variantlcsh:QH426-470chaperoning systemMutantunderdiagnosed chaperonopathiesDiseaseBiology03 medical and health sciences0302 clinical medicinehuman genomeGeneticsMissense mutationGeneGenetics (clinical)Hsp60 genetic chaperonopathieOriginal ResearchGeneticschemistry.chemical_classificationHsp60 genetic chaperonopathieshuman genomesHsp60 gene variantsAmino acidlcsh:Genetics030104 developmental biologychemistry030220 oncology & carcinogenesisMolecular MedicineHSP60Human genomeIdentification (biology)Frontiers in Genetics
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Hsp60 Post-translational Modifications: Functional and Pathological Consequences.

2020

Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis. In addition to this canonical role, Hsp60 plays many others beyond the mitochondria, for instance in the cytosol, plasma-cell membrane, extracellular space, and body fluids. These non-canonical functions include participation in inflammation, autoimmunity, carcinogenesis, cell replication, and other cellular events in health and disease. Thus, Hsp60 is a multifaceted molecule with a wide range of cellular and tissue locations and functions, which is noteworthy because there is only one hsp60 gene. The questio…

0301 basic medicinechaperoninnon-canonical functionsReviewMitochondrioncanonical functionsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrychaperonopathies03 medical and health sciences0302 clinical medicineUbiquitinMolecular Bioscienceslcsh:QH301-705.5Molecular Biologybiologycanonical functions chaperonin Hsp60 non-canonical functions post-translation modificationChemistryfungiCitrullinationCell cycleHsp60Cell biology030104 developmental biologylcsh:Biology (General)Mitochondrial permeability transition pore030220 oncology & carcinogenesisChaperone (protein)biology.proteinPhosphorylationHSP60post-translation modificationFrontiers in molecular biosciences
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GENETIC NEUROCHAPERONOPATHIES ASSOCIATED WITH CCT5 AND HSP60 VARIANTS: ANALYSIS OF THEIR MOLECULAR ANATOMY AND POSSIBLE PATHOGENIC IMPLICATIONS

2022

Settore BIO/17 - IstologiaMISSENSE MUTATIONMITOCHONDRIAPROTEOSTASISMOLECULAR DYNAMICSCHAPERONE SYSTEMCCT5HSP60GENETIC NEUROCHAPERONOPATHIESBIOINFORMATICS ANALYSIS
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